Soluble FCγ receptors

Fridman, Wolf Herman; Teillaud, Jean‐Luc; Bouchard, Caroline; Teillaud, Christophe; Astier, Anne; Tartour, Éric; Galon, Jérôme; Mathiot, Claire; Sautès, Catherine

doi:10.1002/jlb.54.5.504

Cited by 61 publications

(45 citation statements)

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“…Alternative splicing and proteolytic cleavage of membrane-associated FcR have been shown to generate soluble forms of these receptors (sFcR) (19). For example, alternative splicing results in the generation of a TM-deleted Fc␥RIIb2 mRNA (termed Fc␥RIIb3), providing a third isoform encoded by the single murine Fc␥RII gene (8,20).…”

Section: Identification and Characterization Of A Fcr Homolog In An Ementioning

confidence: 99%

Identification and Characterization of a FcR Homolog in an Ectothermic Vertebrate, the Channel Catfish (Ictalurus punctatus)

Stafford

Wilson

Nayak

et al. 2006

The Journal of Immunology

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An FcR homolog (IpFcRI), representing the first such receptor from an ectothermic vertebrate, has been identified in the channel catfish (Ictalurus punctatus). Mining of the catfish expressed sequence tag databases using mammalian FcR sequences for CD16, CD32, and CD64 resulted in the identification of a teleost Ig-binding receptor. IpFcRI is encoded by a single-copy gene containing three Ig C2-like domains, but lacking a transmembrane segment and cytoplasmic tail. The encoded Ig domains of IpFcRI are phylogenetically and structurally related to mammalian FcR and the presence of a putative Fc-binding region appears to be conserved. IpFcRI-related genomic sequences are also present in both pufferfish and rainbow trout, indicating the likely presence of a soluble FcR in other fish species. Northern blot and qualitative PCR analyses demonstrated that IpFcRI is primarily expressed in IgM-negative leukocytes derived from the lymphoid kidney tissues and PBL. Significantly lower levels of IpFcRI expression were detected in catfish clonal leukocyte cell lines. Using the native leader, IpFcRI was secreted when transfected into insect cells and importantly the native IpFcRI glycoprotein was detected in catfish plasma using a polyclonal Ab. Recombinant IpFcRI binds catfish IgM as assessed by both coimmunoprecipation and cell transfection studies and it is presumed that it functions as a secreted FcR akin to the soluble FcR found in mammals. The identification of an FcR homolog in an ectothermic vertebrate is an important first step toward understanding the evolutionary history and functional importance of vertebrate Ig-binding receptors.

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Section: Identification and Characterization Of A Fcr Homolog In An Ementioning

confidence: 99%

Identification and Characterization of a FcR Homolog in an Ectothermic Vertebrate, the Channel Catfish (Ictalurus punctatus)

Stafford

Wilson

Nayak

et al. 2006

The Journal of Immunology

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“…Complement receptor Type I (CD35) [86,87] cleavage Hyaluronate R (CD44) [88] CD58 [89] GPI IgER (Fc⑀RII, CD23) [90,91] cleavage IgGR (Fc␥RII) [92] I ICAM-1 (CD54) [93][94][95] I ICAM-3 (CD50) [96] ?cleavage Transforming growth factor ␤RIII [97,98] cleavage Epidermal growth factor R (c-erb B) [99][100][101][102] splicing I Vascular endothelial growth factor R [103] splicing I…”

Section: Mechanisms Of Soluble Receptor Actionmentioning

confidence: 99%

Soluble receptors in human disease

Heaney

Golde

1998

Journal of Leukocyte Biology

155

132

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“…Soluble forms of both FcgRIIIA and FcgRIIIB derived from the membrane receptors following proteolysis have been identified in plasma and other biological fluids of mice and humans [13][14][15]. The shedding of FcgRIIIA isoform involves mainly matrix metalloproteinases (MMPs), whereas the FcgRIIIB is released by serine proteases and MMP cleavage [16,17].…”

Section: Introductionmentioning

confidence: 99%

Interaction of Human Immunoglobulin G with CD16 on Natural Killer Cells: Ligand Clearance, FcγRIIIA Turnover and Effects of Metalloproteinases on FcγRIIIA‐Mediated Binding, Signal Transduction and Killing‡

Moţa¹,

Moldovan²,

Călugăru³

et al. 2004

Scand J Immunol

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Human natural killer (NK) cells express low-affinity Fc immunoglobulin G (IgG) receptor (FcgRIIIA/CD16). The binding of monomeric IgG (mIgG) and F(ab 0 ) 2 fragments of 3G8 anti-CD16 monoclonal antibody (mAb) to FcgRIIIA was investigated by flow cytometry. Over 90% of NK cells bound endogenous IgG, and during incubation at 37 C, the FcgRIIIA occupancy decreased slowly. Approximately 90% of NK cells bind mIgG or F(ab 0 ) 2 fragments of 3G8 anti-CD16 mAb. The calculated half-time (T 1/2 ) of in vitro mIgG dissociation from FcgRIIIA was 130 min. By cross-linking the mIgG ligand with F(ab 0 ) 2 fragments of anti-human IgG antibody, the T 1/2 decreases to 85 min. In kinetics study, it has been shown that 125 I-mIgG bound to FcgRIIIA is slowly released in the culture supernatant, maybe eluted at acid pH, or partially internalized and degraded. The binding of IgG to FcgRIIIA was increased by 53.8% on cells cultured in the presence of RU36156, a matrix metalloproteinase (MMP) inhibitor. Furthermore, an increase in phosphorylation of Lyn tyrosine kinase, after cross-linking of mIgG-FcgRIIIA complex, was observed on NK cells treated with RU36156. When the FcgRIIIA was occupied by mIgG, the capacity of NK cells to kill K562 target cells was decreased by RU36156, because the MMP inhibitor protects CD16 from proteolysis. Our data demonstrate that binding of mIgG to human NK cells is followed by ligand dissociation and/or internalization, enzymatic degradation and exocytosis. The RU36156 MMP inhibitor protects FcgRIIIA from cleavage, augments NK-cell activation and may interfere in their killing capacity.

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Soluble FCγ receptors

Cited by 61 publications

References 0 publications

Identification and Characterization of a FcR Homolog in an Ectothermic Vertebrate, the Channel Catfish (Ictalurus punctatus)

Identification and Characterization of a FcR Homolog in an Ectothermic Vertebrate, the Channel Catfish (Ictalurus punctatus)

Soluble receptors in human disease

Interaction of Human Immunoglobulin G with CD16 on Natural Killer Cells: Ligand Clearance, FcγRIIIA Turnover and Effects of Metalloproteinases on FcγRIIIA‐Mediated Binding, Signal Transduction and Killing‡

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